What is the role of non-native intermediates of beta-lactoglobulin in protein folding?

The mechanism of alpha --> beta transition in folding of beta -lactoglobuli n is discussed based on free energy landscape analysis of a long lattice mo del. It is found that helical propensity of beta -lactoglobulin is driven b y conformational entropy and is intrinsically coded in its native structure . We propose a view on a role of folding intermediate, which is "on-pathway " but rich in non-native structures. The present results suggest that the n ative structure topology plays an important role in alpha --> beta transiti on.